Human Gene TUBB (uc011gui.2) Description and Page Index
  Description: Homo sapiens tubulin, beta class I (TUBB), mRNA.
RefSeq Summary (NM_178014): This gene encodes a beta tubulin protein. This protein forms a dimer with alpha tubulin and acts as a structural component of microtubules. Mutations in this gene cause cortical dysplasia, complex, with other brain malformations 6. Alternative splicing results in multiple splice variants. There are multiple pseudogenes for this gene on chromosomes 1, 6, 7, 8, 9, and 13. [provided by RefSeq, Jun 2014].
Transcript (Including UTRs)
   Position: chr6_mann_hap4:2,036,251-2,041,289 Size: 5,039 Total Exon Count: 4 Strand: +
Coding Region
   Position: chr6_mann_hap4:2,036,378-2,040,268 Size: 3,891 Coding Exon Count: 4 

Page IndexSequence and LinksUniProtKB CommentsGenetic AssociationsCTDMicroarray
RNA StructureProtein StructureOther SpeciesmRNA DescriptionsPathwaysOther Names
Model InformationMethods
Data last updated: 2013-06-14

+  Sequence and Links to Tools and Databases
  Press "+" in the title bar above to open this section.

-  Comments and Description Text from UniProtKB
  ID: TBB5_HUMAN
DESCRIPTION: RecName: Full=Tubulin beta chain; AltName: Full=Tubulin beta-5 chain;
FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
SUBUNIT: May interact with RNABP10 (By similarity). Interacts with MX1 (By similarity). Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Interacts with PIFO.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in spleen, thymus and immature brain.
DOMAIN: The highly acidic C-terminal region may bind cations such as calcium.
PTM: Some glutamate residues at the C-terminus are polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules (Probable).
SIMILARITY: Belongs to the tubulin family.
WEB RESOURCE: Name=Wikipedia; Note=Tubulin entry; URL="http://en.wikipedia.org/wiki/Tubulin";

+  Genetic Association Studies of Complex Diseases and Disorders
  Press "+" in the title bar above to open this section.

+  Comparative Toxicogenomics Database (CTD)
  Press "+" in the title bar above to open this section.

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

+  mRNA Secondary Structure of 3' and 5' UTRs
  Press "+" in the title bar above to open this section.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR013838 - Beta-tubulin_BS
IPR002453 - Beta_tubulin
IPR008280 - Tub_FtsZ_C
IPR000217 - Tubulin
IPR018316 - Tubulin/FtsZ_2-layer-sand-dom
IPR023123 - Tubulin_C
IPR017975 - Tubulin_CS
IPR003008 - Tubulin_FtsZ_GTPase

Pfam Domains:
PF00091 - Tubulin/FtsZ family, GTPase domain
PF03953 - Tubulin/FtsZ family, C-terminal domain

SCOP Domains:
52490 - Tubulin nucleotide-binding domain-like
55307 - Tubulin C-terminal domain-like

Protein Data Bank (PDB) 3-D Structure

3QNZ
- X-ray Chimera

3QO0
- X-ray Chimera
Chimera help

ModBase Predicted Comparative 3D Structure on P07437
FrontTopSide
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
Genome BrowserGenome BrowserNo orthologNo orthologNo orthologNo ortholog
Gene DetailsGene Details    
Gene SorterGene Sorter    
Jackson LabRGD    
Protein Sequence     
Alignment     

+  Descriptions from all associated GenBank mRNAs
  Press "+" in the title bar above to open this section.

+  Biochemical and Signaling Pathways
  Press "+" in the title bar above to open this section.

+  Other Names for This Gene
  Press "+" in the title bar above to open this section.

+  Gene Model Information
  Press "+" in the title bar above to open this section.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.